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Information on EC 3.2.1.11 - dextranase
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3.2.1.11 dextranaseSpecify your search results
Word Map
- 3.2.1.11
- dextrans
- streptococcus
-
dental
- glucans
- plaque
- penicillium
- caries
- leuconostoc
- sobrinus
- dextransucrase
- isomaltose
-
water-insoluble
-
cariogenic
- mesenteroides
-
colon-specific
- lipomyces
- downei
- sanguis
-
glucosyltransferases
- funiculosum
- salivarius
- mutanase
- synthesis
- medicine
- starkeyi
- isomaltotriose
- agriculture
- degradation
- nutrition
- drug development
- isomalto-oligosaccharides
- biotechnology
- food industry
-
glucan-binding
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dextranase, endodextranase, endo-dextranase, extracellular dextranase, aodex, alpha-glucanase, dex410, tpdex, smdex, dex49a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,6-alpha-D-glucan-6-glucanohydrolase
6-alpha-D-glucan 6-glucanohydrolase
alpha-1,6-D-glucan 6-glucanohydrolase
alpha-1,6-D-glucan-6-glucanohydrolase
Alpha-1,6-glucan-6-glucanohydrolase
alpha-D-1,6-glucan-6-glucanohydrolase
-
-
-
-
AODex
Dex
DexA
dextran hydrolase
-
-
-
-
dextranase
dextranase DL 2
-
-
-
-
DL 2
-
-
-
-
endo-dextranase
endodextranase
Fjoh_4430
LSD1
SmDex
Teth39_0264
TLDex
TPDex
additional information
Alpha-1,6-glucan-6-glucanohydrolase
-
-
-
-
endo-dextranase
-
-
-
-
endodextranase
-
-
-
-
additional information
the enzyme belongs to the glycoside hydrolase family (GH) 66
additional information
the enzyme belongs to the glycoside hydrolase family (GH) 66
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dextran + H2O = dextran fragment 1 + dextran fragment 2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
6-alpha-D-glucan 6-glucanohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-70-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
dextran + H2O
D-glucose + isomaltose + isomalto-oligosaccharides
-
-
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
dextran + H2O
isomaltotetraose
-
-
plus small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 714
-
?
dextran + H2O
isomaltotetraose + cycloisomaltooligosaccharides
-
main products are isomaltotetraose and small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7-14
-
?
dextran T100 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
-
?
dextran T2000 + H2O
isomaltooligosaccharides
-
very high hydrolytic affinity, 100% activity with 3% (w/v) dextran T2000
-
-
?
dextran T2000 + H2O
isomaltotriose + isomaltotetraose + isomaltopentaose
-
-
main end-products
-
?
dextran T3 + H2O
isomaltose + isomaltotriose + D-glucose
-
65.17% activity compared to dextran T70
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose
88% activity compared to dextran T70
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose + D-glucose
-
98.5% activity compared to dextran T70
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
-
?
dextran T5 + H2O
isomaltose + isomaltotriose + D-glucose
-
65.54% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose + D-glucose
-
99.62% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
90.78% activity compared to dextran T250
-
-
?
dextran T60-90 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
90.19% activity compared to dextran T250
-
-
?
dextran T70 + H2O
isomaltooligosaccharides
-
96% of the activity with dextran T500
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
100% activity
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose + D-glucose
-
100% activity
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
-
?
glucan + H2O
D-glucose + isomaltose + isomaltotriose + ?
Achaetomiella gracilis
-
from Streptococcus sobrinus K1-R
-
-
?
isomaltohexaose + H2O
D-glucose + isomaltose + isomaltotriose + isomaltotetraose + isomaltopentaose
-
-
-
?
Sephacryl S-300 + H2O
?
-
4.02% activity compared to dextran T250
-
-
?
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
-
-
-
?
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
-
-
-
?
4-nitrophenyl alpha-isomaltopentoside + H2O
?
-
-
-
?
4-nitrophenyl alpha-isomaltotetraoside + H2O
?
-
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
dextran + H2O
?
-
extent of hydrolysis of 5-aminosalicylic acid-dextran conjugates (secondary amines) by dextranase is in part controlled by the degree of oxidation and by the amount of conjugated 5-aminosalicylic acid. Less oxidised dextrans (12%) conjugating proportionally less 5-aminosalicylic acid are successfully hydrolysed by dextranase
-
-
?
dextran + H2O
?
-
extent of hydrolysis of 5-aminosalicylic acid-dextran conjugates (secondary amines) by dextranase is in part controlled by the degree of oxidation and by the amount of conjugated 5-aminosalicylic acid. Less oxidised dextrans (12%) conjugating proportionally less 5-aminosalicylic acid are successfully hydrolysed by dextranase
-
-
?
dextran + H2O
?
-
substrate dextran T-20 98.9%, dextran 20000 91.3%, dextran T-70 98.3%, dextran T-500 85.1%, dextran T-2000 86.7% relative activity, respectively
-
-
?
dextran + H2O
?
-
substrate dextran T-20 98.9%, dextran 20000 91.3%, dextran T-70 98.3%, dextran T-500 85.1%, dextran T-2000 86.7% relative activity, respectively
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
D-glucose + isomaltotriose + isomaltose + isomaltooligosaccharide
-
-
-
-
?
dextran + H2O
D-glucose + isomaltotriose + isomaltose + isomaltooligosaccharide
-
-
-
-
?
dextran + H2O
glucose + maltose + maltotriose + maltotetraose
-
-
final products
-
?
dextran + H2O
glucose + maltose + maltotriose + maltotetraose
-
-
final products
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D1
isomaltobiose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D2
isomaltotetraose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D1
isomaltobiose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D2
isomaltotetraose-isomaltodecaose
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + isomaltooligosaccharides
with 4 mg/ml dextran, isomaltooligosaccharides with degrees of polymerization of 3 and 4 are present at the beginning of the reaction, and D-glucose and isomaltose are produced by the end of the reaction
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + isomaltooligosaccharides
with 4 mg/ml dextran, isomaltooligosaccharides with degrees of polymerization of 3 and 4 are present at the beginning of the reaction, and D-glucose and isomaltose are produced by the end of the reaction
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
Penicillium cyclopium CICC-4022
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
dextran + H2O
malto-oligosaccharides
dextran of 5000 Da, 0.5%
-
-
?
dextran + H2O
malto-oligosaccharides
dextran of 5000 Da, 0.5%
-
-
?
dextran + H2O
oligosaccharides
Achaetomiella gracilis
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
Ascospirella lutea ATCC 9644
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
maltose, maltotriose and other maltosaccharides
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
substrates are dextrans of 15-25 kDa and 410 kDa. Ten units of dextranase can reduce dextran content by 67% in 24 h and 56% in 72 h from sugarcane juice of cane variety CoS 86032
-
-
?
dextran + H2O
oligosaccharides
-
substrates are dextrans of 15-25 kDa and 410 kDa. Ten units of dextranase can reduce dextran content by 67% in 24 h and 56% in 72 h from sugarcane juice of cane variety CoS 86032
-
-
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran T10 + H2O
isomaltose + isomaltotriose
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
88.64% activity compared to dextran T250
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
88.64% activity compared to dextran T250
-
-
?
dextran T20 + H2O
isomaltooligosaccharides
-
90% of the activity with dextran T500
-
-
?
dextran T20 + H2O
isomaltooligosaccharides
-
68.64% activity compared to dextran T2000
-
-
?
dextran T20 + H2O
isomaltose + isomaltotriose + D-glucose
-
90.64% activity compared to dextran T70
-
-
?
dextran T20 + H2O
isomaltose + isomaltotriose + D-glucose
Penicillium cyclopium CICC-4022
-
90.64% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + D-glucose
-
97% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + D-glucose
Penicillium cyclopium CICC-4022
-
97% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
87.48% activity compared to dextran T250
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
87.48% activity compared to dextran T250
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
?
dextran T250 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
100% activity
-
-
?
dextran T250 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
100% activity
-
-
?
dextran T40 + H2O
isomaltooligosaccharides
-
91% of the activity with dextran T500
-
-
?
dextran T40 + H2O
isomaltooligosaccharides
-
72.96% activity compared to dextran T2000
-
-
?
pullulan + H2O
?
4% activity compared to dextran T70
-
-
?
soluble starch + H2O
?
Penicillium cyclopium CICC-4022
-
20.83% activity compared to dextran T70
-
-
?
additional information
?
-
-
no activity with starch, cellulose, glycol chitin, chitin, Sephadex G10, sucrose, and maltose
-
-
?
additional information
?
-
-
no activity with starch, cellulose, glycol chitin, chitin, Sephadex G10, sucrose, and maltose
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the alpha-1,6 glycosidic bond. Poor substrate: starch. No substrate: pullulan
-
-
?
additional information
?
-
-
no activity toward Sepharose 6B, beta-cyclodextrin, chitosan, maltose, or sucrose
-
-
?
additional information
?
-
no substrates: trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The enzyme additionally catalyzes disproportionation of isomaltose to form isomaltooligosaccharides
-
-
?
additional information
?
-
-
no substrates: trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The enzyme additionally catalyzes disproportionation of isomaltose to form isomaltooligosaccharides
-
-
?
additional information
?
-
no substrates: trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The enzyme additionally catalyzes disproportionation of isomaltose to form isomaltooligosaccharides
-
-
?
additional information
?
-
glycosyl hydrolase family 66 enzymes may be classified into three types: dextranases showing only dextranolytic activity, dextranases catalyzing hydrolysis with low cyclization activity, and cycloisomaltooligosaccharide glucanotransferases showing cycloisomaltooligosaccharide-forming activity with low dextranolytic activity
-
-
?
additional information
?
-
no or very low activity on substrates isomaltose, isomaltotriose, isomaltotetraose
-
-
?
additional information
?
-
glycosyl hydrolase family 66 enzymes may be classified into three types: dextranases showing only dextranolytic activity, dextranases catalyzing hydrolysis with low cyclization activity, and cycloisomaltooligosaccharide glucanotransferases showing cycloisomaltooligosaccharide-forming activity with low dextranolytic activity
-
-
?
additional information
?
-
no or very low activity on substrates isomaltose, isomaltotriose, isomaltotetraose
-
-
?
additional information
?
-
-
the enzyme has no effects on cellulose, sucrose, chitin, chitosan and beta-cyclodextrin
-
-
?
additional information
?
-
Penicillium cyclopium CICC-4022
-
the enzyme has no effects on cellulose, sucrose, chitin, chitosan and beta-cyclodextrin
-
-
?
additional information
?
-
-
dextrans with a maximum degree of oxidation (93%) giving maximum conjugation of 5-aminosalicylic acid are resistant to dextranase hydrolysis
-
-
?
additional information
?
-
-
dextrans with a maximum degree of oxidation (93%) giving maximum conjugation of 5-aminosalicylic acid are resistant to dextranase hydrolysis
-
-
?
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
?
additional information
?
-
-
enzyme hydrolyzed alpha-1,6 glucosidic bonds but not alpha-1,4 glucosidic bonds
-
-
?
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
?
additional information
?
-
-
enzyme hydrolyzed alpha-1,6 glucosidic bonds but not alpha-1,4 glucosidic bonds
-
-
?
additional information
?
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
?
additional information
?
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
?
additional information
?
-
-
no activity on blue dextran brain heart infusion agar plates
-
-
?
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
?
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
?
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
?
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
?
additional information
?
-
-
no activity on blue dextran brain heart infusion agar plates
-
-
?
additional information
?
-
no activity toward 4-nitrophenyl alpha-isomaltotrioside
-
-
?
additional information
?
-
-
no activity toward 4-nitrophenyl alpha-isomaltotrioside
-
-
?
additional information
?
-
no activity toward 4-nitrophenyl alpha-isomaltotrioside
-
-
?
additional information
?
-
-
enzyme influences glucan synthesis, linkage remodeling and branching
-
-
?
additional information
?
-
-
no activity towards beta-cyclodextrin, chitin, Sepharose 6B, chitosan, and sucrose. Low activity towards soluble starch
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
dextran T40 + H2O
isomaltose + isomaltotriose
88% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
100% activity
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
Penicillium cyclopium CICC-4022
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
73% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
pullulan + H2O
?
4% activity compared to dextran T70
-
-
?
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
?
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
?
additional information
?
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
?
additional information
?
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
K+
Li+
Mg2+
Mn2+
Na+
Ni2+
additional information
Fe2+
stimulates activity of the dextransucrase-dextranase fusion protein
K+
stimulates activity of the dextransucrase-dextranase fusion protein
Li+
stimulates activity of the dextransucrase-dextranase fusion protein
Mg2+
activity increases to 125% in the presence of 1 mM Mg2+
Ni2+
stimulates activity of the dextransucrase-dextranase fusion protein
Ni2+
activity increases to 125% in the presence of 1 mM Ni2+
additional information
-
no effects on enzyme activity by K+, Mg2+, and Ca2+ on both free and immobilized enzymes
additional information
Ca2+, Li+, K+, and Na+ (with chloride) do not show appreciable effects on activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aflatoxin B1
inhibits dextranase activities of CYP3A4-expressing cultures, maximum inhibition of 22% at 2 microg/ml. Only negligibly inhibits strain INVSC1 expressing dextranase
aflatoxin G1
substantially less inhibitory towards dextranase activities of CYP3A4-expressing cultures than aflatoxin B1, showing a maximum inhibition of about 12% at 2 microg/ml, whereas strain INVSC1 expressing dextranase is only marginally inhibited
Na+
-
85% inhibition of the free enzyme, 60% inhibition of the immobilized enzyme
T-2 toxin
100% inhibition at 10 microg/ml of dextranase activities of CYP3A4-expressing cultures and strain INVSC1
Ca2+
-
5 mM, isoform D-I 71% residual activity, isoform D-II 83% residual activity
Cu2+
-
93% inhibition of the free enzyme, 56.5% inhibition of the immobilized enzyme
Fe2+
-
41.5% inhibition of the free enzyme, 18% inhibition of the immobilized enzyme
Fe2+
-
5 mM, isoform D-I 47% residual activity, isoform D-II 38% residual activity
Hg2+
-
complete inhibition of the free enzyme and the immobilized enzyme
Mn2+
-
23% inhibition of the free enzyme, 6% inhibition of the immobilized enzyme
Mn2+
-
5 mM, isoform D-I 67% residual activity, isoform D-II 63% residual activity
Pb2+
-
5 mM, isoform D-I 23% residual activity, isoform D-II 10% residual activity
Zn2+
-
21% inhibition of the free enzyme, 8% inhibition of the immobilized enzyme
additional information
-
not inhibited by Mn2+, Co2+, Zn2+, Ni2+, PCMB and EDTA
-
additional information
-
teeth rinsing product reagents, including carboxybenzene, ethanol, sodium fluoride, and xylitol have no effects on enzyme activity
-
additional information
Chaetomium erraticum
-
for successful adsorption, enzyme to bentonite ratios greater than 0.4 (w/w) have to be used as lower ratios lead to 90% enzyme inactivation due to bentonite contact
-
additional information
-
Zn2+, Co2+, Ni2+, Fe3+ and EDTA show no obvious inhibition at 1 mM
-
additional information
-
not inhibited by dithiothreitol, 2-mercaptoethanol and EDTA
-
additional information
-
stable to Cu2+, Fe3+, Mg2+, Zn2+, EDTA and iodoacetamide
-
additional information
-
not inhibited by Mn2+, Co2+, Al3+, Mg2+ and EDTA
-
additional information
-
degree of enzyme inactivation declines with increasing ratio dextranase per dextranase adsorbate bentonite, at a ratio below 0.5: (w/w) only one half of the initial activity is retained
-
additional information
no significant inhibition of dextranase activities of CYP3A4-expressing cultures and strain INVSC1 at concentrations of 2, 20, 200, and 2000 ng/ml by deoxynivalenol, fumonisin B1, and ochratoxin A
-
additional information
-
no significant inhibition of dextranase activities of CYP3A4-expressing cultures and strain INVSC1 at concentrations of 2, 20, 200, and 2000 ng/ml by deoxynivalenol, fumonisin B1, and ochratoxin A
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Chaetomium erraticum
-
bentonite carriers exhibit high monolayer protein and activity loads at pH 4.0 and after pH-shift to 5.4. If dextranase is adsorbed at pH 4.1 and hydroxyapatite is washed several times with buffer at pH 5.4 reveals highest activity yield so far (28%). Other selected carriers used are hydroxyapatite and Streamline DEAE. In general, immobilization yields are low and in case of DEAE the rather high particle size is problematic. Porous Eupergit differs only moderately in activity using low molecular weight substrate, whereas macroporous Eupergit reveals enhanced activity for high molecular weight substrates. Activation of the carbohydrate moiety of dextranase by metaperiodate results in active silica gels, whereas the activation of alginate via Woodwards reagent K exhibits extremely low activities
-
additional information
-
highest immobilization efficiency at 200 mg Eupergit C with a ratio of activity of immobilized enzyme to the activity of soluble enzyme of 90%, higher amounts of Eupergit C yield lower immobilization efficiency. Immobilization duration increases immobilization efficiency
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alveolar Bone Loss
Effects of two dextranase preparations on dental caries and alveolar bone loss in hamsters.
Colonic Neoplasms
Colon specific enzyme responsive oligoester crosslinked dextran nanoparticles for controlled release of 5-fluorouracil.
Crohn Disease
Dextran and 5-aminosalicylic acid (5-ASA) conjugates: synthesis, characterisation and enzymic hydrolysis.
Dental Caries
Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste.
Dental Caries
Characterization of a marine-derived dextranase and its application to the prevention of dental caries.
Dental Caries
Effect of dextranase prepared from Spicaria violacea on dental caries in the hamster.
Dental Caries
Effects of two dextranase preparations on dental caries and alveolar bone loss in hamsters.
Dental Caries
Inhibition of rat dental caries by dextranase from a strain of Spicaria violacea.
Dental Caries
Optimization of Fungal Dextranase Production and Its Antibiofilm Activity, Encapsulation and Stability in Toothpaste.
Dental Caries
Renaturation of dextranase activity from culture supernatant fluids of Streptococcus sobrinus after sodium dodecylsulfate polyacrylamide gel electrophoresis.
Dental Caries
The development and application of dextranase in the prevention of dental caries.
Dental Caries
[Effects of dextranase, monofluorophosphate, and their combination on the reduction of dental caries and plaque in rats]
Dental Plaque
1. The effect of a dextranase mouthwash on dental plaque in young adults and children.
Dental Plaque
A novel dextranase gene from the marine bacterium Bacillus aquimaris S5 and its expression and characteristics.
Dental Plaque
Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste.
Dental Plaque
Effect of dextranase on the extracellular polysaccharide synthesis of Streptococcus mutans; chemical and scanning electron microscopy studies.
Dental Plaque
Effects of dextranase from Spicaria violaceae (IFO 6120) on the polysaccharides produced by oral streptococci and on human dental plaque.
Dental Plaque
Expression, purification and characterization of a cold-adapted dextranase from marine bacteria and its ability to remove dental plaque.
Dental Plaque
Immobilization of Dextranase on Nano-Hydroxyapatite as a Recyclable Catalyst.
Dental Plaque
In vitro adsorption of dextranase by dental plaque and buccal mucosa, and its oral retention after rinsing the mouth.
Dental Plaque
Metabolism of the polysaccharides of human dental plaque. I. Dextranase activity of streptococci, and the extracellular polysaccharides synthesized from sucrose.
Dental Plaque
Metabolism of the polysaccharides of human dental plaque: release of dextranase in batch cultures of Streptococcus mutans.
Dental Plaque
The effect of a bacterial dextranase on human dental plaque formation and gingivitis development.
Dental Plaque
The effect of dextranase on the release of reducing sugars from dental plaque.
Dental Plaque
The influence of mutanase and dextranase on the production and structure of glucans synthesized by streptococcal glucosyltransferases.
Dental Plaque
The influence of the probiotic Streptococcus salivarius M18 on indices of dental health in children: a randomised double-blind placebo-controlled trial.
Dental Plaque
The Marine Catenovulum agarivorans MNH15 and Dextranase: Removing Dental Plaque.
Dental Plaque
[Effects of dextranase from a strain of Spicaria species on the polysaccharides prepared from human dental plaque (author's transl)]
Dental Plaque
[In vitro and clinical effects of Chaetomium gracile dextranase on the release of reducing sugar and on the reduction of dental plaque]
Dental Plaque
[Scanning electron microscope study on the removal of artificial dental plaque treated with a bacteriolytic enzyme from Streptomyces globisporus--its synergistic effects with dextranase and lysozyme (author's transl)]
Dental Plaque
[The clinical effect of dextranase from spicaria violaceae on human dental plaque (author's transl)]
Dental Plaque
[The effect of dentifrice containing Chaetomium gracile dextranase on the reduction of dental plaque (2)--the time series analysis of variance]
Dental Plaque
[The in vitro effects of dextranase on dental plaque produced by Streptococcus mutans]
Endocarditis
Bacterial adherence in the pathogenesis of endocarditis. Interaction of bacterial dextran, platelets, and fibrin.
Endocarditis
Dextranase enhances antibiotic efficacy in experimental viridans streptococcal endocarditis.
Endocarditis
Enzymatic modification of glycocalyx in the treatment of experimental endocarditis due to viridans streptococci.
Gingivitis
The effect of a bacterial dextranase on human dental plaque formation and gingivitis development.
Hematuria
Enzymolysis of glomerular immune deposits in vivo with dextranase/protease ameliorates proteinuria, hematuria, and mesangial proliferation in murine experimental IgA nephropathy.
Periodontal Diseases
The retardation of spontaneous periodontal disease and the prevention of caries in hamsters with dextranase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.05
Dextran
-
pH not specified in the publication, temperature not specified in the publication
3.2
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 5.0
3.3
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 5.0
5.9
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 4.0
7.1
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 6.0
7.14
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 4.0
8.3
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 3.0
9.1
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 3.0
9.1
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 6.0
87.1
Dextran
Chaetomium erraticum
-
ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C
0.0095
dextran T2000
in 40 mM sodium acetate buffer (pH4.3) at 55°C
-
additional information
Dextran
Km value 0.374 mg/ml, p-h 4.5, 37°C
additional information
Dextran
KF241867
Km value of native enzyme, 4.38 mg/ml, of immobilzed enzyme, 9.92 mg/ml, respectively, pH 7.0, 50°C
additional information
Dextran
Km value 1.77 g/l, pH 6.0, 50°C, dextran with molecular weight from 60000 to 90000 Da
additional information
dextran 742CB
-
Km value is 2.9 mg/ml, pH 5.2, 70°C
-
additional information
dextran T2000
-
Km value is 6.4 mg/ml, pH 5.2, 70°C
-
additional information
dextran T500
-
Km value is 2.5 mg/ml, pH 5.2, 70°C
-
additional information
additional information
-
0.06 microgram/ml, dextran
-
additional information
additional information
-
0.26 g/l, dextran
-
additional information
additional information
Chaetomium erraticum
-
KM-values of soluble and adsorbed enzymes do not differ significantly
-
additional information
additional information
-
0.9 g (500 kDa dextran) per l
-
additional information
additional information
-
1.3 g (500 kDa dextran) per l
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.7
Dextran
Chaetomium erraticum
-
ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
76.78
Dextran
Chaetomium erraticum
-
ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C
additional information
dextran 742CB
-
Km value is 1.25ml per mg and s, pH 5.2, 70°C
-
additional information
dextran T2000
-
kcat_/Km value is 5.9 ml per mg and s, pH 5.2, 70°C
-
additional information
dextran T500
-
Km value is 3.3 ml per mg and s, pH 5.2, 70°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11.9
3.02
purified recombinant enzyme SmDex95, the 95 kDa variant, pH 5.0, temperature not specified in the publication
43
8.21
purified recombinant enzyme SmDex90, the 90 kDa variant, pH 5.0, temperature not specified in the publication
90
additional information
additional information
Achaetomiella gracilis
-
60603.3 dextranase units/mg, concentrated dextranase 1, one dextranase unit is the amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4
additional information
Achaetomiella gracilis
-
8290.8 dextranase units/mg, concentrated dextranase 3, factory 2, amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4
additional information
Achaetomiella gracilis
-
8402.8 dextranase units/mg, concentrated dextranase 3, factory 1, amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4
additional information
Chaetomium erraticum
-
6356.3 dextranase units/mg, one unitis the amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4
additional information
-
release of 78.5 mg of Remazol Blue R-250 dye/min at 50°C
additional information
activities of recombinant fusion protein and of wild-type dextranase in fermentation, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
4.5 - 5.5
4.6
5 - 6
5.2
5.3
5.4
5.4 - 5.8
5.5
5.8
6.5
additional information
-
optimum pH for activity 4.5-5.5 is not affected by immobilization
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
4 - 6
4 - 8
4.5 - 9.5
the enzyme is inactive below pH 4.5 and above pH 9.5
5 - 5.5
5 - 6.4
5 - 6.5
5.5 - 8.3
70-100% activity at pH 6.0-8.0, 50% activity at pH 5.5 and pH 8.3
3 - 6
-
with pH ranged from 3.0 to 6.0, the relative enzyme activity is higher than 72.67%
3 - 6
-
approx. 50% of maximal activity at pH 6.3, complete loss of activity above pH 7.5
5 - 6.4
great loss in activity below and above that values, recombinant wild-type dextranase and engineered fusion protein DSXR
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
35 - 40
-
dex1 from strain Dex40-8 and dex2 from strain Dex50-2,inactive above 50°C
37
40
40 - 45
43.3 - 54.4
45
50
55
60
65
70
additional information
-
ranges for both soluble or immobilized enzyme between 30-35°C
60
Chaetomium erraticum
-
optimum temperature under ultrasound/microwave irradiation shock treatment
60
-
enzyme retains more than 70% maximal activity after incubation at 57°C for 9.5 h in the absence of substrate
60
temperature optima of mutants are similar to that of the wild-type
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
approx. 50% of maximal activity at 30°C, dramatic decrease in activity above 45°C
25 - 60
over 80% activity retained within the range of 37-50°C, 50% of maximal activity at 25°C and 60°C
25 - 65
-
the enzyme activity successively increases with temperature from 25 to 55°C. Rising the temperatures from 55 to 60 and 65°C results in a decrease in enzyme activity by 25% and 66%, respectively
30 - 60
-
approx. 35% of maximal activity at 30°C, approx. 10% of maximal activity at 60°C
35 - 60
-
when temperature varying from 35 to 60°C, the relative activity is always higher than 54.55%
50 - 60
55 - 60
60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
4.5
4.6
4.9
5.7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achaetomiella gracilis
aerobic bacterium SRI 2125
commentary isolated from the hot environs of a raw sugar factory
-
-
brenda
aerobic bacterium SRI 2126
commentary isolated from the hot environs of a raw sugar factory
-
-
brenda
aerobic bacterium SRI 2128
commentary isolated from the hot environs of a raw sugar factory
-
-
brenda
aerobic bacterium SRI 2140
commentary isolated from the hot environs of a raw sugar factory
-
-
brenda
anaerobic thermophilic bacterium AB11A
gram-negative, thermophilic, anaerobic, isolated from the non-volcanic low-temperature field, the Great Artesian Basin in Queensland
-
-
brenda
Chaetomium erraticum
isolated from sugar-cane farm soil, gene aodex
UniProt
brenda
dextranase D1, dextranase D2, dextranase D3 and dextranase D4
-
-
brenda
Achaetomiella gracilis
concentrated dextranase 1 and non-concentrated dextranase 3
-
-
brenda
isolated from sugar-cane farm soil, gene aodex
UniProt
brenda
strain MT8148, serotype c, and strain MT8148, serotype f
SwissProt
brenda
strain SL1, serotype d, and strain 6715DP, serotype g
SwissProt
brenda
isolated from an active volcanic zone high-temperature field at the biothermal springs at Rotoruna, New Zealand
-
-
brenda
isolated from an active volcanic zone high-temperature field at the biothermal springs at Rotoruna, New Zealand
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
cells are cultivated in brain-heart infusion medium
brenda
additional information
-
cells are cultivated in brain-heart infusion medium
brenda
additional information
-
cells are cultivated in brain-heart infusion medium
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
dextranase hydrolyzes the alpha-1,6 glucosidic bond of dextran to release isomaltooligosaccharides, as endo-dextranase, produced by various microorganisms including bacteria, yeast, and fungi
physiological function
-
dextranase hydrolyzes the alpha-1,6 glucosidic bond of dextran to release isomaltooligosaccharides, as endo-dextranase, produced by various microorganisms including bacteria, yeast, and fungi
-
additional information
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
additional information
-
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
additional information
-
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
-
Show AA Sequence and Transmembrane Helices (110 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
114000
130000
160000
170000
175000
23000
26500
44000
59000
60000
64000
66000
68000
68300
69000
70000
71000
76000
77000
78000
79000
80000
89000
89800
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
94537
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
95400
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
97000
68300
x * 71000, SDS-PAGE, x * 68300, about, sequence calculation
71000
x * 71000, SDS-PAGE, x * 68300, about, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
multimer
additional information
?
x * 71000, SDS-PAGE, x * 68300, about, sequence calculation
?
-
x * 71000, SDS-PAGE, x * 68300, about, sequence calculation
-
?
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
?
-
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
-
additional information
the enzyme comprises four regions from the N- to C-termini: N-terminal variable region, N-VR, conserved region, CR, glucan-binding site, GBS, and C-terminal variable region, C-VR
additional information
-
the enzyme comprises four regions from the N- to C-termini: N-terminal variable region, N-VR, conserved region, CR, glucan-binding site, GBS, and C-terminal variable region, C-VR
additional information
-
the enzyme comprises four regions from the N- to C-termini: N-terminal variable region, N-VR, conserved region, CR, glucan-binding site, GBS, and C-terminal variable region, C-VR
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
10-12% of dextranase mass corresponds to carbohydrate in the form of N-linked oligosaccharide chains
glycoprotein
-
3 potential N-glycosylation sites, differences in glycosylation profiles between native and recombinant dextranase
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure, based on PDB entry 1ogm.1
hanging drop vapor diffusion method, using 0.2 M MgCl2, 0.1 M HEPES (pH 7.5), and 30% (w/v) polyethylene glycol 400
crystal structure of the conserved fragment from residue Gln100 to Ile732, devoid of its N- and C-terminal variable regions, 1.6 A resolution. Structural domain N possesses an immunoglobulin-like beta-sandwich fold, domain A contains the enzyme's catalytic module, comprising a (beta/alpha)8-barrel, and domain C forms a beta-sandwich structure containing two Greek key motifs. In the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties is observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites in the catalytic cleft. The complexed structure with suicide substrate 4',5'-epoxypentyl-alpha-D-glucopyranoside reveals that the epoxide ring reacts to form a covalent bond with the Asp385 side chain. Asp385 is the catalytic nucleophile and Glu453 is the acid/base of the double displacement mechanism
crystal structure of apo-Dex49A and Dex49A complexed with product at 1.8 A and 1.65 A, respectively
crystal structures of the wild type and catalytic mutant D312G in complex with isomaltohexaose. The enzyme consists of a catalytic domain comprising an (beta/alpha)8-barrel and two beta-domains located at both N- and C-terminal ends. The isomaltohexaose molecule is bound across the catalytic site, showing the existence of six subsites (-4 to +2) in the catalytic cleft. Marked movement of the W376 side-chain along with loop 6, which is the side wall component of the cleft at subsite +1, is observed to occupy subsite +1
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D279C/S289C
T245C/N248C
-
the mutant shows a more than 3°C improvement on its optimal temperature compared to the wild type enzyme
D189A
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
D340G
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
E412Q
D189A
-
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
-
D340G
-
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
-
E412Q
-
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
-
A356F
the mutant exhibits improved thermostability compared to the wild type enzyme
G355F
the mutant exhibits improved thermostability compared to the wild type enzyme
S354F
the mutant exhibits improved thermostability compared to the wild type enzyme
S357F
the mutant exhibits improved thermostability compared to the wild type enzyme
S357F/G355F
the mutant exhibits improved thermostability compared to the wild type enzyme
A356F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
G355F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
S354F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
S357F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
S357F/G355F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
T558H
the mutation affects the hydrolytic activities of the enzyme. The mutant increases the proportion of isomaltooligosaccharide with degrees of polymerization of 5 in hydrolysates following reactions with 4 mg/ml dextran
T563N
the mutation affects the hydrolytic activities of the enzyme
W279A
the mutation affects the hydrolytic activities of the enzyme
W279A/T563N
the mutations affect the hydrolytic activities of the enzyme
W279F
the mutation affects the hydrolytic activities of the enzyme
W279F/T563N
the mutations affect the hydrolytic activities of the enzyme
T558H
-
the mutation affects the hydrolytic activities of the enzyme. The mutant increases the proportion of isomaltooligosaccharide with degrees of polymerization of 5 in hydrolysates following reactions with 4 mg/ml dextran
-
W279A
-
the mutation affects the hydrolytic activities of the enzyme
-
W279A/T563N
-
the mutations affect the hydrolytic activities of the enzyme
-
W279F
-
the mutation affects the hydrolytic activities of the enzyme
-
W279F/T563N
-
the mutations affect the hydrolytic activities of the enzyme
-
D312G
additional information
D279C/S289C
-
the mutant shows a more than 13°C improvement on its optimal temperature compared to the wild type enzyme
D279C/S289C
-
the mutant shows a more than 3°C improvement on its optimal temperature compared to the wild type enzyme
E412Q
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
additional information
-
immobilization of dextranase on several carriers by entrapment and covalent binding with cross-linking. Entrapment in sodium alginate with Ca2+. Dextranase immobilized on bovine serum albumin with a cross-linking agent shows the highest activity and considerable immobilization yield of 66.7%. The optimum pH of the immobilized enzyme is shifted to pH 6.0 as compared to the free enzyme pH 5.5. The optimum temperature of the reaction is at 60°C for both free and immobilized enzyme. Thermal and pH stability are significantly improved by the immobilization process. Km of the immobilized dextranase is higher than that of the free dextranase, while Vmax of the immobilized enzyme is lower than that of the free dextranase. The immobilized enzyme is able to retain 76% of the initial catalytic activity after 5.0 cycles
additional information
dexI mutants with improved thermostability. In terms of their relative specific activity towards dextran, noticeable differences among mutants showing increased, similar or reduced enzyme activity as compared to wild-type
additional information
-
dexI mutants with improved thermostability. In terms of their relative specific activity towards dextran, noticeable differences among mutants showing increased, similar or reduced enzyme activity as compared to wild-type
additional information
a C-terminal truncated enzyme, residues Ala39-Ser1304, has 50% wild-type activity
additional information
-
a C-terminal truncated enzyme, residues Ala39-Ser1304, has 50% wild-type activity
-
additional information
generation of an engineered fusion enzyme of dextransucrase, from dsrBCB4 gene from Leuconostoc mesenteroides B-1299CB4, and Arthrobacter oxydans dextranase, i.e. DSXR. DSXR is potentially useful for reliable production of long isomalto-oligosaccharides from sucrose by a one-step reaction
additional information
-
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
additional information
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
additional information
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
additional information
-
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
-
additional information
-
loss of activity in N-terminal deletion mutants
additional information
generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
additional information
-
generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
additional information
-
generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 7
3.5 - 7
4.3 - 10
stable from pH 4.3-10.0 after incubation at 4°C for 20 h, activity drops sharply above pH 10.0 and below pH 4.3
701864
4.5 - 4.75
4.8 - 9
5 - 9
-
the enzyme exhibits stability with more than 80% relative activity at pH 5.0-9.0
752286
5.5 - 11
Achaetomiella gracilis
-
-
135747
5.5 - 7.5
5.5 - 8.5
the enzyme has a stable pH range from 5.5 to 8.5
750900
additional information
-
immobilized enzyme is more stable in lower pH (3.5-4.0) and higher pH (6.0-7.5) ranges
678011
2.5 - 7
-
the relative enzymatic activity of dextranase stored at pH 2.5-7.0 for 1 h and 24 h, is 89.22% and 84.58%, respectively
750873
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
the enzyme retains greater than 85% residual activity after storage at 20-50°C (pH 5.5) for 1 h. The enzyme is thermally stable at temperatures below 50°C and has a half-life of 45 days at 28°C
20 - 75
-
the enzyme exhibits thermostability in the range of 20-50°C over an incubation period of 1.5 h. The enzyme loses more than 50% activity at 55°C and 100% activity over the range of 60-75°C. The half-life at 55°C is 52 min
30 - 60
the enzyme has a thermostable temperature of 30°C, a half-life of 30 min at 55°C and shows 9.66% residual activity after 30 min at 60°C
35
40
45
45 - 50
-
after 60 min 45°C and 50°C, the dextranase activity remains stable with the values being 98.09% and 62.21% of relative enzymatic activity, respectively
50
55
60
60 - 65
over 75% of the original activity is sustained at 60°C for 4 h, the half-life of the enzyme is 1.5 h at 65°C with pH4.3 in the absence of added dextran
70
-
half-life of the free enzyme is 49.22 min, and of the immobilized enzyme 70.15 min
75
80
additional information
60
-
half-life of the free enzyme is 331.15 min, and of the immobilized enzyme 431.8 min
80
-
half-life of the free enzyme is 4.21 min, and of the immobilized enzyme 30.43 min
additional information
-
immobilized enzyme is more stable at high temperatures
additional information
-
plateau of tolerance to higher temperatures up to 44°C, at higher temperatures rapid decrease of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+, Mn2+, Fe3+, Ni2+, Co2+, Sr2+, Cu2+, EDTA have no effect to enzyme stability
-
matrix-bound stable when stored as acetone-dried powder or as a suspension in acetate buffer for about 3 weeks at 4°C
-
non-concentrated dextranase unstable at refridgerator temperatures
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Methanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20øC, acetate buffer pH 5.4, 10% (w/v) sucrose, 10% (v/v) glycerol, no activity loss over 560 days (crude enzyme preparation)
-
23-27C in the dark
4°C to -20°C, 0.02 M acetate buffer (pH 5.5), over 2 months, no loss of activity
-
4°C, 2 mM NaN3, 6 months, the purified SmDex90 is proteolytically degraded to more than seven polypeptides of 23-70 kDa during long storage
non-concentrated dextranase very unstable at storage in a refrigeerator
Achaetomiella gracilis
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
17.56fold by cation-exchange chromatography, 18.18fold followed by Ni-affinity chromatography
-
ammonium sulfate precipitation and ion-exchange column chromatography
ammonium sulfate precipitation and Sephacryl S-300 HR gel filtration
-
ammonium sulfate, 20% polyethylene glycol 6000, interphase adsorption, DEAE-Sepharose
-
native enzyme by anion exchange chromatography, recombinant His-tagged enzyme 16fold from Escherichia coli by nickel affinity chromatography
partial
recombinant form with six histidine residues tagged in the C-terminus partially purified on Ni-NTA column
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) CodonPlus-RIL by nickel affinity chromatography, ultrafilatration, and hydrophobic interaction and anion exchange chromatography
the dextransucrase-dextranase fusion protein is partially purified by DEAE-Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
dex1 gene from Dex70-1B and Dex70-34, expression in Escherichia coli TOP10F
-
dex1 gene from strain Dex40-8 and strain Dex50-2, expression in Escherichia coli TOP10F
-
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) CodonPlus-RIL
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae INVSc1 via fusion of the DNA segment encoding the mature dextranase protein with alpha-factor signal sequence, and insertion into the GAL1-controlled expression vector pYES2/CT (construction of the four dextranase-expressing plasmids pYES2/CT-dex, pYES2/CT-dex-tag, pYES2/CT-alphaF-dex(m) and pYES2/CT-alphaF-dex(m)-tag). Dextranase construct pYESCT2-alphaF-dex(m) introduced into a strain of Saccharomyces cerevisiae expressing the human cytochrome P4503A4 (CYP3A4) and the cognate reductase
expression in Escherichia coli
expression in Pichia pastoris
gene aodex, DNA and amino acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli
gene dex2, expression of the engineered fusion enzyme DSXR in Escherichia coli strain BL21(DE3)pLysS, optimization of protein expression conditions for enhancement of protein production by the effects of three-level-three-factors and their mutual interaction in Escherichia coli
into vector pET-21a(+), recombinant form with six histidine residues tagged in the C-terminus expressed in Escherichia coli strain BL21(DE3)
into vector pPIC9k-His6 and expressed in Pichia pastoris GS115 strain under the control of AOX1 promoter
-
the dextransucrase-dextranase fusion protein is expressed in Escherichia coli BL21(DE3) cells
wild-type dex1 gene directly cloned into NotI and XbaI sites of pEH75 and transformed into Escherichia coli Mach1TM-T1 cells. Dex1 coding regions from wild-type and thermostable mutants PCR-amplified from pEH75 and cloned into pET-45b(+) and transformed into Escherichia coli expression host BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
degradation
drug development
-
fractionated dextrans possess commercial interest in cosmetics, drug formulations, vaccines, cryoprotectants
food industry
medicine
nutrition
synthesis
degradation
KF241867
crosslinking of dextranase on chitosan hydrogel microspheres. A shift in optimum pH and temperature from 7.0 to 7.5 and 50 to 60°C is observed after immobilization, respectively. Recycling efficiency, thermal stability, and activation energy distinctly improve after immobilization, whereas anchoring of substrate at the active site of the soluble dextranase exhibits an increase in Km with no change in Vmax after crosslinking
degradation
Chaetomium erraticum
-
the hydrolysis of dextran under ultrasound/microwave irradiation shock treatment is significantly higher than those performed under ultrasound, microwave irradiation shock and conventional thermal incubation at all conditions studied. The maximum hydrolysis rate is observed when ultrasound/microwave irradiation shock (ultrasound of 50 W combined with microwave irradiation shock of 60 W at a sock rate of 20 s/min for 25 min) is used in which the dextran hydrolysis increases by 171.13% compared with routine conventional heating. Vmax and KM values of dextranase under ultrasound/microwave irradiation shock treatment are higher than those under ultrasound, microwave irradiation shock and conventional thermal incubation
degradation
Priestia megaterium KIBGE-IB31
-
crosslinking of dextranase on chitosan hydrogel microspheres. A shift in optimum pH and temperature from 7.0 to 7.5 and 50 to 60°C is observed after immobilization, respectively. Recycling efficiency, thermal stability, and activation energy distinctly improve after immobilization, whereas anchoring of substrate at the active site of the soluble dextranase exhibits an increase in Km with no change in Vmax after crosslinking
-
food industry
-
the use of the dextranase enzyme is the most efficient method for hydrolyzing the dextrans at sugar mills
food industry
Achaetomiella gracilis
-
alpha-dextranase removes dextran by 46.6% in mixed sugarcane juice and 14.1% in clarified sugarcane juice
food industry
-
the enzyme is used for dextran elimination in sugar production process
food industry
Achaetomiella gracilis CGMCC3 3783
-
alpha-dextranase removes dextran by 46.6% in mixed sugarcane juice and 14.1% in clarified sugarcane juice
-
food industry
-
the enzyme is used for dextran elimination in sugar production process
-
medicine
-
partial hydrolysis of native dextran in the preparation of blood substitutes
medicine
-
partial hydrolysis of native dextran in the preparation of blood substitutes
medicine
-
enzyme plays a role in controlling both the adhesive properties of extracellular glucan and the ability to utilize extracellular glucan as a nutrient source
medicine
-
less oxidised dextrans conjugating proportionally less 5-aminosalicylic acid successfully hydrolysed by dextranase, suggest their potential applications for the treatment of Crohns disease in the distal ileum and proximal colon
medicine
-
isoform Dex410 effectively inhibits the Streptococcus mutans biofilm growth in coverage, biomass, and water-soluble glucan by more than 80, 90, and 95%, respectively. For short-term use of 1.5 months in animal experiment, both Dex410 and the commercial mouthwash Biotene have a significant inhibitory effect on caries, while for 3 months use, only Dex410 shows significant inhibitory effect on dental caries
medicine
-
dextranase can inhibit the adhesive ability of Streptomyces mutans. It inhibits biofilm formation and removes previously formed biofilms. The minimum biofilm inhibition and reduction concentrations (MBIC50 and MBRC50) of dextranase are 2 U/ml and 5 U/ml, respectively
medicine
-
enzyme impedes the formation of Streptococcus mutans biofilm to some extent. Teeth rinsing product reagents, including carboxybenzene, ethanol, sodium fluoride, and xylitol have no effects on enzyme activity
medicine
-
dextranase can inhibit the adhesive ability of Streptomyces mutans. It inhibits biofilm formation and removes previously formed biofilms. The minimum biofilm inhibition and reduction concentrations (MBIC50 and MBRC50) of dextranase are 2 U/ml and 5 U/ml, respectively
-
medicine
-
less oxidised dextrans conjugating proportionally less 5-aminosalicylic acid successfully hydrolysed by dextranase, suggest their potential applications for the treatment of Crohns disease in the distal ileum and proximal colon
-
medicine
-
partial hydrolysis of native dextran in the preparation of blood substitutes
-
nutrition
-
evluation of the storage stability of dextranase by adding enzyme protective reagents, i.e. stabilizers and antiseptics. Best stabilizers of dextranase are glycerol (16%), sodium acetate (18%) and sodium citrate (20%). 4-Hydroxybenzoic acid compound sodium acetate (0.05%), sodium D-isoascorbiate (0.03%), and potassium sorbate (0.05%)are the best antiseptics
nutrition
-
evluation of the storage stability of dextranase by adding enzyme protective reagents, i.e. stabilizers and antiseptics. Best stabilizers of dextranase are glycerol (16%), sodium acetate (18%) and sodium citrate (20%). 4-Hydroxybenzoic acid compound sodium acetate (0.05%), sodium D-isoascorbiate (0.03%), and potassium sorbate (0.05%)are the best antiseptics
-
synthesis
-
investigation on various adding times of dextranase to the dextransucrase system to reveal the synergistic processes of dextransucrase and dextranase. Dextranase added into the dextransucrase-sucrose system at different times gives rise to different main dextran products. Dextranase added into sucrose system at the same time with dextransucrase synthesizes low molecular weight dextran targeted to 5 kDa, while dextranase added during the reaction process of dextransucrase directionally prepares dextran with medium Mw of 10 kDa and 20 kDa. The synthesized oligodextrans are mainly composed of alpha-1,6-glycosidic linkages and low alpha-1,3-glycosidic branches
synthesis
-
maximum enzyme production is obtained in a self designed medium (pH 6.0) containing 1% dextran 5000 Da, after 24 h culture incubation at 37°C.High dextranase production is achieved when medium is supplemented with dextran as only carbon source and no enzyme production is found in medium having glucose, sucrose or starch. Dextranase production is inversely proportional to dextran polymer length and extent of branching
synthesis
-
optimal conditions for synthesis of enzyme are 28 h, 8.0, 30°C, and 25% volume of liquid in 100-ml Erlenmeyer flasks, respectively
synthesis
-
optimized culture conditions for dextranase productions are 37°C, pH 10, 32 h, and 20% (v/w) moisture content. The addition of 0.175 mM CrCl3 increases the enzyme production by about 4.5fold
synthesis
-
immobilization of enzyme in Fe3+-cross-linked alginate/carboxymethyl cellulose beads. The immobilization process improves the optimum temperature from 35°C to 45°C. The immobilized enzyme shows its optimum activity for synthesis of dextran in pH range 4.5-5.4 compared to pH 5.4 in case of free form. The immobilization process improve the thermal and pH enzyme stability to great extent. The enzyme retains 60% activity after 15 batch reactions
synthesis
Achaetomiella gracilis
-
alpha-dextranase activity reaches 242.8 U/ml when fermentation conditions are 29°C, pH 6.0 and 220 rpm. Addition of glass beads to fermentation medium after 12 h improves enzyme activity by 135.5%
synthesis
Achaetomiella gracilis
-
culturing Chaetomium gracile in medium containing crude dextran and use of high molecular weight of dextrans results in higher dextranase production. Cells incubated in medium containing glucose as sole carbon source exhibit a high growth rate but do not produce dextranase. Using fed-batch and two-step fermentation strategies, production of 159.5 and 187.0 U/ml, respectively, can be achieved
synthesis
-
optimized culture conditions for dextranase productions are 37°C, pH 10, 32 h, and 20% (v/w) moisture content. The addition of 0.175 mM CrCl3 increases the enzyme production by about 4.5fold
-
synthesis
Achaetomiella gracilis CGMCC3 3783
-
alpha-dextranase activity reaches 242.8 U/ml when fermentation conditions are 29°C, pH 6.0 and 220 rpm. Addition of glass beads to fermentation medium after 12 h improves enzyme activity by 135.5%
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arnold, W.A.; Nguyen, T.B.P.; Mann, L.C.
Purification and characterization of a dextranase from Sporothrix schenckii
Arch. Microbiol.
170
91-98
1998
Sporothrix schenckii, Sporothrix schenckii IP29
brenda
Shimizu, E.; Unno, T.; Ohba, M.; Okada, G.
Purification and characterization of an isomaltotriose-producing endo-dextranase from a Fusarium sp.
Biosci. Biotechnol. Biochem.
62
117-122
1998
Fusarium sp.
brenda
Abdel-Naby, M.A.; Ismail, A.M.S.; Abdel-Fattah, A.M.; Abdel-Fattah, A.F.
Preparation and some properties of immobilized Penicillium funiculosum 258 dextranase
Proc. Biochem.
34
391-398
1999
Talaromyces funiculosus, Talaromyces funiculosus 258
-
brenda
Wanda, S.Y.; Curtiss III, R.
Purification and characterization of streptococcus sobrinus dextranase produced in recombinant Escherichia coli and sequence analysis of the dextranase gene
J. Bacteriol.
176
3839-3850
1994
Streptococcus sobrinus, Streptococcus sobrinus UAB66
brenda
Igarashi, T.; Yakamoto, A.; Goto, N.
Characterization of the dextranase purified from Streptococcus mutans Ingbritt
Microbiol. Immunol.
36
969-976
1992
Streptococcus mutans Ingbritt
brenda
Igarashi, T.; Yakamoto, A.; Goto, N.
Characterization of the dextranase gene (dex) of Streptococcus mutans and its recombinant product in an Escherichia coli host
Microbiol. Immunol.
39
387-391
1995
Streptococcus mutans Ingbritt
brenda
Das, D.K.; Dutta S.K.
Purification, biochemical characterization and mode of action an extracellular endo-dextranase from the culture filtrate of Penicillium lilacinum
Int. J. Biochem. Cell Biol.
28
107-113
1996
Purpureocillium lilacinum
-
brenda
Wynter, C.V.A.; Galea, C.F.; Cox, L.M.; Dawson, M.W.; Patel, B.K.; Hamilton, S.; De Jersey, J.; Inkerman, P.A.
Thermostable dextranases: screening, detection and preliminary characterization
J. Appl. Bacteriol.
19
203-212
1995
anaerobic thermophilic bacterium AB11A, Achaetomiella gracilis, Thermochaetoides thermophila, Achaetomiella virescens, Purpureocillium lilacinum, Talaromyces funiculosus, Thermoanaerobacter sp., aerobic bacterium SRI 2125, aerobic bacterium SRI 2126, aerobic bacterium SRI 2128, aerobic bacterium SRI 2140, thermophilic bacterium DP17, Thermochaetoides thermophila ATCC 58195, Thermoanaerobacter sp. Rt364, Thermochaetoides thermophila ATCC 28076, Achaetomiella virescens ATCC 32319, Talaromyces funiculosus 258
-
brenda
Wellington, J.E.; Shaw, J.M.; Walker, G.J.
Influence of growth rate on the relative activities of free and bound dextranase and dextranase inhibitor in continuous cultures of Streptococcus sobrinus
Microbios
79
121-129
1994
Streptococcus sobrinus, Streptococcus sobrinus UAB66
brenda
Galvez-Mariscal, A.; Lopez-Munguia, A.
Production and characterization of a dextranase from an isolated Paecilomyces lilacinus strain
Appl. Microbiol. Biotechnol.
36
327-331
1991
Purpureocillium lilacinum, Purpureocillium lilacinum 6R
-
brenda
Simonson, L.G.; Liberta, A.E.; Richardson, A.
Characterization of an extracellular dextranase from Fusarium moniliforme
Appl. Microbiol.
30
855-861
1975
Fusarium verticillioides
brenda
Staat, R.H.; Schachtele, C.F.
Characterization of a dextranase produced by an oral strain of Actinomyces israelii
Infect. Immun.
12
556-563
1975
Actinomyces israelii
brenda
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Pseudarthrobacter oxydans, Pseudarthrobacter oxydans KQ11
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Pseudarthrobacter oxydans, Pseudarthrobacter oxydans KQ11
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Esawy, M.; Mansour, S.; Ahmed, E.; Hassanein, N.; El Enshasy, H.
Characterization of extracellular dextranase from a novel halophilic Bacillus subtilis NRC-B233b a mutagenic honey isolate under solid state fermentation
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Characterization of a marine-derived dextranase and its application to the prevention of dental caries
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Wang, X.; Cheng, H.; Lu, M.; Fang, Y.; Jiao, Y.; Li, W.; Zhao, G.; Wang, S.
Dextranase from Arthrobacter oxydans KQ11-1 inhibits biofilm formation by polysaccharide hydrolysis
Biofouling
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Shahid, F.; Aman, A.; Nawaz, M.; Karim, A.; Ul Qader, S.
Chitosan hydrogel microspheres: an effective covalent matrix for crosslinking of soluble dextranase to increase stability and recycling efficiency
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Priestia megaterium (KF241867), Priestia megaterium KIBGE-IB31 (KF241867)
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Gozu, Y.; Ishizaki, Y.; Hosoyama, Y.; Miyazaki, T.; Nishikawa, A.; Tonozuka, T.
A glycoside hydrolase family 31 dextranase with high transglucosylation activity from Flavobacterium johnsoniae
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Flavobacterium johnsoniae (A5FBI1), Flavobacterium johnsoniae, Flavobacterium johnsoniae DSM 2064 (A5FBI1)
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Bashari, M.; Jin, Z.; Wang, J.; Zhan, X.
A novel technique to improve the biodegradation efficiency of dextranase enzyme using the synergistic effects of ultrasound combined with microwave shock
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Chaetomium erraticum
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Zohra, R.R.; Aman, A.; Ansari, A.; Haider, M.S.; Qader, S.A.
Purification, characterization and end product analysis of dextran degrading endodextranase from Bacillus licheniformis KIBGE-IB25
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Bacillus licheniformis (C0HJE3), Bacillus licheniformis KIBGE-IB25 (C0HJE3), Bacillus licheniformis KIBGE-IB25
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Hashem, A.M.; Gamal, A.A.; Hassan, M.E.; Hassanein, N.M.; Esawy, M.A.
Covalent immobilization of Enterococcus faecalis Esawy dextransucrase and dextran synthesis
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Enterococcus faecalis
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Suzuki, N.; Kishine, N.; Fujimoto, Z.; Sakurai, M.; Momma, M.; Ko, J.A.; Nam, S.H.; Kimura, A.; Kim, Y.M.
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Thermoanaerobacter pseudethanolicus (B0KBZ7), Thermoanaerobacter pseudethanolicus, Thermoanaerobacter pseudethanolicus ATCC 33223 (B0KBZ7)
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Identification of catalytic amino acid residues by chemical modification in dextranase
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Virgen-Ortiz, J.; Ibarra-Junquera, V.; Escalante-Minakata, P.; Ornelas-Paz, J.; Osuna-Castro, J.; Gonzalez-Potes, A.
Kinetics and thermodynamic of the purified dextranase from Chaetomium erraticum
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Chaetomium erraticum
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Bhatia, S.; Bhakri, G.; Arora, M.; Batta, S.; Uppal, S.
Kinetic and thermodynamic properties of partially purified dextranase from Paecilomyces lilacinus and its application in dextran removal from cane juice
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Purpureocillium lilacinum
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Sufiate, B.; Soares, F.; Moreira, S.; Gouveia, A.; Cardoso, E.; Braga, F.; de Araujo, J.; de Queiroz, J.
In vitro and in silico characterization of a novel dextranase from Pochonia chlamydosporia
3 Biotech
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Pochonia chlamydosporia (A0A179FQV9)
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Zhang, Y.; Li, R.; Zhang, H.; Wu, M.; Hu, X.
Purification, characterization, and application of a thermostable dextranase from Talaromyces pinophilus
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Talaromyces pinophilus
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Ren, W.; Cai, R.; Yan, W.; Lyu, M.; Fang, Y.; Wang, S.
Purification and characterization of a biofilm-degradable dextranase from a marine bacterium
Mar. Drugs
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Catenovulum sp.
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Li, K.; Lu, H.; Hang, F.; Li, S.; Liu, J.
Improved dextranase production by Chaetomium gracile through optimization of carbon source and fermentation parameters
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Achaetomiella gracilis
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Zhang, Z.; Liu, J.; Ma, S.; Lu, H.; Hang, F.; Huang, P.; Li, K.
Enhancement of catalytic performance of alpha-dextranase from Chaetomium gracile through optimization and suitable shear force
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78-87
2018
Achaetomiella gracilis, Achaetomiella gracilis CGMCC3 3783
-
brenda
Klahan, P.; Okuyama, M.; Jinnai, K.; Ma, M.; Kikuchi, A.; Kumagai, Y.; Tagami, T.; Kimura, A.
Engineered dextranase from Streptococcus mutans enhances the production of longer isomaltooligosaccharides
Biosci. Biotechnol. Biochem.
82
1480-1487
2018
Streptococcus mutans (Q54443), Streptococcus mutans, Streptococcus mutans ATCC 700610 (Q54443)
brenda
Yang, L.; Zhou, N.; Tian, Y.
Purification, characterization, and biocatalytic potential of a novel dextranase from Chaetomium globosum
Biotechnol. Lett.
40
1407-1418
2018
Chaetomium globosum
brenda
Huang, R.; Zhong, L.; Xie, F.; Wei, L.; Gan, L.; Wang, X.; Liao, A.
Purification, characterization and degradation performance of a novel dextranase from Penicillium cyclopium CICC-4022
Int. J. Mol. Sci.
20
1360
2019
Penicillium cyclopium, Penicillium cyclopium CICC-4022
brenda
Ren, W.; Liu, L.; Gu, L.; Yan, W.; Feng, Y.L.; Dong, D.; Wang, S.; Lyu, M.; Wang, C.
Crystal structure of GH49 dextranase from Arthrobacter oxidans KQ11 identification of catalytic base and improvement of thermostability using semirational design based on B-factors
J. Agric. Food Chem.
67
4355-4366
2019
Pseudarthrobacter oxydans (A0A059VLI3), Pseudarthrobacter oxydans, Pseudarthrobacter oxydans KQ11 (A0A059VLI3)
brenda
Florez Guzman, G.Y.; Hurtado, G.B.; Ospina, S.A.
New dextransucrase purification process of the enzyme produced by Leuconostoc mesenteroides IBUN 91.2.98 based on binding product and dextranase hydrolysis
J. Biotechnol.
265
8-14
2018
Chaetomium erraticum
brenda
Netsopa, S.; Niamsanit, S.; Araki, T.; Kongkeitkajorn, M.; Milintawisamai, N.
Purification and characterization including dextran hydrolysis of dextranase from Aspergillus allahabadii X26
Sugar Tech.
21
329-340
2019
Aspergillus allahabadii, Aspergillus allahabadii X26
-
brenda
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